NDLI: In situ Raman spectroscopy distinguishes between reversible and irreversible thiol modifications in l-cysteine

Content Provider	Royal Society of Chemistry (RSC)
Author	Fanchini, Giovanni Bazylewski, Paul Divigalpitiya, Ranjith
Copyright Year	2017
Abstract	In this study we introduce in situ Raman spectroscopy as an effective tool to distinguish between reversible and irreversible thiol modifications in L-cysteine, the most critical host for sulphydryls in proteins and enzymes. We place special emphasis on the conditions under which the formation and breakage of disulphide bonds is reversible and produces free thiol groups. Thiol groups from L-cysteine are highly reactive and are frequently converted into disulphide bonds via reaction with mercaptans, including S-methyl methanethiosulfonate (MMTS). It was previously claimed that disulphide groups can be reversibly introduced in and eliminated from L-cysteine in order to restore a free thiol group, using a reductant such as tris(2-carboxyethyl)phosphine (TCEP). Raman spectroscopy is found to effectively monitor the formation and subsequent breaking of disulphide bonds, and demonstrates that although TCEP is effective in breaking disulphide bonds, an excess of TCEP is required to reversibly form free thiol groups from L-cysteine. These results will be critical for cysteine–metal bonding investigations. Our Raman mode assignment in MMTS and TCEP also provides a benchmark for future studies using these compounds.
Starting Page	2964
Ending Page	2970
Page Count	7
File Format	HTM / HTML PDF
ISSN	20462069
Volume Number	7
Issue Number	5
Journal	RSC Advances
DOI	10.1039/c6ra25879d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Thiol Cysteine Hyderabad Multi-Modal Transport System Raman MMTS Raman spectroscopy TCEP
Content Type	Text
Resource Type	Article
Subject	Chemistry Chemical Engineering

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